Linked Life Data

667130

Source:http://linkedlifedata.com/resource/pubmed/id/667130

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1978-9-29
pubmed:abstractText
UDPgalactose : glycoprotein galactosyltransferase in normal human skin fibroblast homogenates has been assayed using ovalbumin as an acceptor. The activity in the homogenate fraction sedimenting between 51 300 X g and 105 000 X g was enhanced by the addition of a number of catonic polypeptides of L-configuration but not by those of D-configuration. In contrast to the enhancing effect of poly(L-lysine), poly(L-glutamic acid) inhibited the activity. Poly(D-glutamic acid) had no effect. Cationic or anionic amino acid derivatives, spermine or spermidine had no effect on activity. The enhancement of transferase activity by poly(L-arginine) is probably due to an increase in V for UDPgalactose and ovalbumin. The implication of these results for the regulation of glycoprotein synthesis in cultivated skin fibroblasts and for the pathogenesis of cystic fibrosis is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
541
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
435-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Enhancement of UDPgalactose: glycoprotein galactosyltransferase in cultured human skin fibroblasts by cationic polypeptides.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.